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. 2017 Mar 15;7:201. doi: 10.1038/s41598-017-00143-6

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© The Author(s) 2017

This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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Identification of post-translational modification (PTM) residues in core histone proteins of bladder cancer cells following heat shock protein 90 inhibitor treatment. The illustration of identified PTM sites on the core histones in 5637 cells in response to AUY922 (A) and ganetespib (B) exposure. The identified PTM sites on the core histones are numbered and highlighted. *Indicates novel histone marks identified in this study. A, acetyl; B, butyryl; C, citrulline; D, dimethyl; G, O-GlcNAcyl; H, 2-hydroxyisobutyryl; M, monomethyl; Ma, malonyl; O, oxidation; P, phosphoryl; Pr, propionyl; S, succinyl; T, trimethyl; U, ubiquityl. (C) An MS/MS spectrum of a tryptic peptide histone H4K20 lysine-butyrylated peptide _RK(bu)VLRDNIQGITKPAIR. (D) An MS/MS spectrum of a tryptic peptide histone H2BK46 lysine-propionylated peptide _VLK(pr)QVHPDTGISSK. (E) An MS/MS spectrum of a tryptic peptide histone H4R23 arginine-trimethylated peptide _KVLR(me3)DNIQGITKPAIR. (F) An MS/MS spectrum of a tryptic peptide histone H3K122 lysine-succinylated peptide _RVTIMPK(su)DIQLAR.